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Atomistry » Calcium » PDB 4ggb-4gpe » 4ghe » |
Calcium in PDB 4ghe: Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang ResolutionEnzymatic activity of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution
All present enzymatic activity of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution:
1.13.11.15; Protein crystallography data
The structure of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution, PDB code: 4ghe
was solved by
E.G.Kovaleva,
J.D.Lipscomb,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ghe:
The structure of Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution
(pdb code 4ghe). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution, PDB code: 4ghe: Calcium binding site 1 out of 1 in 4gheGo back to Calcium Binding Sites List in 4ghe
Calcium binding site 1 out
of 1 in the Structure of Y257F Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.60 Ang Resolution
Mono view Stereo pair view
Reference:
E.G.Kovaleva,
J.D.Lipscomb.
Structural Basis For the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen Activation. Biochemistry V. 51 8755 2012.
Page generated: Sat Dec 12 04:47:59 2020
ISSN: ISSN 0006-2960 PubMed: 23066739 DOI: 10.1021/BI301115C |
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